Magnesium in PDB 7rhv: Aspergillus Fumigatus Enolase

All present enzymatic activity of Aspergillus Fumigatus Enolase:
4.2.1.11;

The structure of Aspergillus Fumigatus Enolase, PDB code: 7rhv was solved by S.Nguyen, J.B.Bruning, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.39 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	67.174, 83.969, 84.661, 90, 97.56, 90
R / Rfree (%)	16 / 21.4

The binding sites of Magnesium atom in the Aspergillus Fumigatus Enolase (pdb code 7rhv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Aspergillus Fumigatus Enolase, PDB code: 7rhv:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Aspergillus Fumigatus Enolase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Aspergillus Fumigatus Enolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:19.6 occ:1.00 O A:HOH672 2.0 16.3 1.0 O A:HOH673 2.0 22.5 1.0 OE2 A:GLU297 2.1 17.6 1.0 OD2 A:ASP246 2.1 19.5 1.0 OD2 A:ASP322 2.1 15.4 1.0 O A:HOH849 2.2 22.6 1.0 CG A:ASP246 3.0 17.8 1.0 CG A:ASP322 3.2 21.7 1.0 OD1 A:ASP246 3.2 16.1 1.0 CD A:GLU297 3.2 17.2 1.0 CB A:ASP322 3.6 10.3 1.0 NZ A:LYS398 4.0 13.8 1.0 CG A:GLU297 4.0 15.3 1.0 OE1 A:GLN167 4.0 27.2 1.0 OE1 A:GLU297 4.1 16.0 1.0 OD2 A:ASP298 4.2 19.4 1.0 O A:HOH832 4.3 31.1 1.0 OD1 A:ASP322 4.3 18.7 1.0 CB A:ASP246 4.3 18.1 1.0 OE2 A:GLU168 4.3 20.8 1.0 NZ A:LYS347 4.5 15.7 1.0 CD2 A:LEU345 4.5 12.3 1.0 CB A:ALA248 4.8 18.6 1.0 CD A:GLU168 4.9 17.8 1.0 CG A:ASP298 4.9 19.4 1.0

Magnesium binding site 2 out of 2 in the Aspergillus Fumigatus Enolase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Aspergillus Fumigatus Enolase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:18.4 occ:1.00 O B:HOH731 2.1 16.6 1.0 OD2 B:ASP322 2.1 19.5 1.0 O B:HOH623 2.1 16.3 1.0 OE2 B:GLU297 2.1 20.9 1.0 O B:HOH876 2.1 17.9 1.0 OD2 B:ASP246 2.2 21.7 1.0 CG B:ASP246 3.1 18.2 1.0 CG B:ASP322 3.1 20.2 1.0 CD B:GLU297 3.2 16.9 1.0 OD1 B:ASP246 3.3 16.9 1.0 CB B:ASP322 3.5 14.2 1.0 CG B:GLU297 4.0 15.2 1.0 NZ B:LYS398 4.1 16.1 1.0 OE1 B:GLU297 4.2 18.5 1.0 OD2 B:ASP298 4.2 19.9 1.0 OD1 B:ASP322 4.2 17.9 1.0 O B:HOH620 4.3 33.8 1.0 OE2 B:GLU168 4.3 19.4 1.0 NE2 B:GLN167 4.3 15.7 1.0 CB B:ASP246 4.4 16.3 1.0 CD2 B:LEU345 4.5 13.1 1.0 NZ B:LYS347 4.5 13.6 1.0 O B:HOH846 4.7 29.6 1.0 CG B:ASP298 4.9 19.2 1.0 CD B:GLU168 4.9 17.7 1.0 CB B:ALA248 5.0 15.2 1.0

S.Nguyen, B.Jovcevski, J.Q.Truong, T.L.Pukala, J.B.Bruning. A Structural Model of the Human Plasminogen and Aspergillus Fumigatus Enolase Complex. Proteins V. 90 1509 2022.
ISSN: ESSN 1097-0134
PubMed: 35247004
DOI: 10.1002/PROT.26331